Structural highlights
Function
TRYP_PIG
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The first crystal structure of an active autolysate form of porcine alpha-trypsin (APT), a two-chain molecule obtained from the limited autolysis of porcine beta-trypsin at position Lys145-Ser146, has been determined. APT crystallizes in space group P2(1)2(1)2(1) with one protein molecule in the asymmetric unit. The structure was solved by molecular replacement followed by refinement using X-PLOR to an R factor of 0.200 and an R(free) of 0.285 for 8.0-1.8 A data with r.m.s deviations from ideal values of 0.01 A and 1.7 degrees for bond lengths and bond angles, respectively. Comparison with inactive autolysate porcine epsilon-trypsin (EPT) and porcine beta-trypsin in complex with bittergourd trypsin inhibitor (MCT) revealed a small but systematic directional chain shift around the active-site residues from APT to EPT to MCT.
The first structure at 1.8 A resolution of an active autolysate form of porcine alpha-trysoin.,Johnson A, Krishnaswamy S, Sundaram PV, Pattabhi V Acta Crystallogr D Biol Crystallogr. 1997 May 1;53(Pt 3):311-5. PMID:15299934[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Johnson A, Krishnaswamy S, Sundaram PV, Pattabhi V. The first structure at 1.8 A resolution of an active autolysate form of porcine alpha-trysoin. Acta Crystallogr D Biol Crystallogr. 1997 May 1;53(Pt 3):311-5. PMID:15299934 doi:10.1107/S0907444997000358
